STRING allows inspection of the interaction evidence for any given network. Choose any of the viewers above (disabled if not applicable in your network).

Nodes:

Network nodes represent proteins

splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.

Node Color

colored nodes:query proteins and first shell of interactors

white nodes:second shell of interactors

Node Content

empty nodes:proteins of unknown 3D structure

filled nodes:some 3D structure is known or predicted

Edges:

Edges represent protein-protein associations

associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding each other.

Known Interactions

from curated databases

experimentally determined

Predicted Interactions

gene neighborhood

gene fusions

gene co-occurrence

Others

textmining

co-expression

protein homology

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Cooccurence

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[Homology]

Score

def

Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions (174 aa)

Predicted Functional Partners:

fmt

methionyl-tRNA formyltransferase; Modifies the free amino group of the aminoacyl moiety of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by- (I) promoting its recognition by IF2 and (II) impairing its binding to EFTu-GTP (318 aa)

0.977

rplQ

50S ribosomal protein L17 (117 aa)

0.909

Dehly_1009

Mg chelatase subunit ChlI (505 aa)

0.883

rplV

50S ribosomal protein L22; The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome (112 aa)

0.874

Dehly_0644

HAD-superfamily hydrolase (216 aa)

0.871

clpP

Endopeptidase Clp; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (205 aa)

0.767

rsmH

S-adenosyl-methyltransferase MraW; Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA (356 aa)

0.626

folD

Methenyltetrahydrofolate cyclohydrolase; Catalyzes the oxidation of 5,10- methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10- formyltetrahydrofolate (295 aa)

a tab-delimited file describing the names, domains and annotated functions of the network proteins

Browse interactions in tabular form:

node1

node2

node1 accession

node2 accession

node1 annotation

node2 annotation

score

Dehly_0590

Dehly_1147

Dehly_0590

Dehly_1147

Ribulose-phosphate 3-epimerase

Methyltransferase

0.497

Dehly_0590

def

Dehly_0590

Dehly_0643

Ribulose-phosphate 3-epimerase

Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions

0.592

Dehly_0590

fmt

Dehly_0590

Dehly_1722

Ribulose-phosphate 3-epimerase

methionyl-tRNA formyltransferase; Modifies the free amino group of the aminoacyl moiety of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by- (I) promoting its recognition by IF2 and (II) impairing its binding to EFTu-GTP

0.577

Dehly_0644

def

Dehly_0644

Dehly_0643

HAD-superfamily hydrolase

Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions

0.871

Dehly_1009

clpP

Dehly_1009

Dehly_0684

Mg chelatase subunit ChlI

Endopeptidase Clp; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins

0.422

Dehly_1009

def

Dehly_1009

Dehly_0643

Mg chelatase subunit ChlI

Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions

0.883

Dehly_1147

Dehly_0590

Dehly_1147

Dehly_0590

Methyltransferase

Ribulose-phosphate 3-epimerase

0.497

Dehly_1147

def

Dehly_1147

Dehly_0643

Methyltransferase

Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions

0.602

Dehly_1147

rsmH

Dehly_1147

Dehly_1232

Methyltransferase

S-adenosyl-methyltransferase MraW; Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA

0.405

clpP

Dehly_1009

Dehly_0684

Dehly_1009

Endopeptidase Clp; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins

Mg chelatase subunit ChlI

0.422

clpP

def

Dehly_0684

Dehly_0643

Endopeptidase Clp; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins

Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions

0.767

def

Dehly_0590

Dehly_0643

Dehly_0590

Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions

Ribulose-phosphate 3-epimerase

0.592

def

Dehly_0644

Dehly_0643

Dehly_0644

Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions

HAD-superfamily hydrolase

0.871

def

Dehly_1009

Dehly_0643

Dehly_1009

Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions

Mg chelatase subunit ChlI

0.883

def

Dehly_1147

Dehly_0643

Dehly_1147

Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions

Methyltransferase

0.602

def

clpP

Dehly_0643

Dehly_0684

Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions

Endopeptidase Clp; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins

0.767

def

fmt

Dehly_0643

Dehly_1722

Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions

methionyl-tRNA formyltransferase; Modifies the free amino group of the aminoacyl moiety of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by- (I) promoting its recognition by IF2 and (II) impairing its binding to EFTu-GTP

0.977

def

folD

Dehly_0643

Dehly_0815

Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions

Methenyltetrahydrofolate cyclohydrolase; Catalyzes the oxidation of 5,10- methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10- formyltetrahydrofolate

0.624

def

rplQ

Dehly_0643

Dehly_1068

Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions

50S ribosomal protein L17

0.909

def

rplV

Dehly_0643

Dehly_1092

Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions

50S ribosomal protein L22; The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome

0.874

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Network Stats

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Functional enrichments in your networkNote: some enrichments may be expected here (why?)

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Statistical background

For the above enrichment analysis, the following statistical background is assumed: